Fluorine in PDB 5v7y: Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Protein crystallography data
The structure of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu, PDB code: 5v7y
was solved by
N.J.Schnicker,
M.Dey,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
63.40 /
2.05
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
50.238,
106.826,
81.056,
90.00,
103.65,
90.00
|
R / Rfree (%)
|
16.1 /
20.9
|
Other elements in 5v7y:
The structure of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
(pdb code 5v7y). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 9 binding sites of Fluorine where determined in the
Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu, PDB code: 5v7y:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
Fluorine binding site 1 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 1 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F303
b:32.4
occ:1.00
|
F1
|
A:TFA303
|
0.0
|
32.4
|
1.0
|
C2
|
A:TFA303
|
1.4
|
25.2
|
1.0
|
F2
|
A:TFA303
|
2.2
|
37.9
|
1.0
|
F3
|
A:TFA303
|
2.2
|
26.9
|
1.0
|
C1
|
A:TFA303
|
2.4
|
20.4
|
1.0
|
OXT
|
A:TFA303
|
2.7
|
16.9
|
1.0
|
O
|
A:GLY194
|
3.0
|
14.9
|
1.0
|
C
|
A:GLY194
|
3.1
|
22.7
|
1.0
|
CG2
|
A:THR159
|
3.4
|
12.2
|
1.0
|
N
|
A:GLY195
|
3.4
|
16.7
|
1.0
|
O
|
A:TFA303
|
3.5
|
22.0
|
1.0
|
CD2
|
A:HIS193
|
3.7
|
15.9
|
1.0
|
CA
|
A:GLY195
|
3.8
|
16.1
|
1.0
|
CA
|
A:GLY194
|
3.9
|
18.0
|
1.0
|
OG1
|
A:THR159
|
4.0
|
10.9
|
1.0
|
CB
|
A:THR159
|
4.1
|
13.5
|
1.0
|
N
|
A:GLY194
|
4.2
|
13.0
|
1.0
|
CA
|
A:THR159
|
4.3
|
11.7
|
1.0
|
NE2
|
A:HIS193
|
4.6
|
14.5
|
1.0
|
CG
|
A:HIS193
|
4.7
|
15.1
|
1.0
|
C
|
A:HIS193
|
4.8
|
15.0
|
1.0
|
N3
|
A:IMD302
|
4.8
|
16.2
|
1.0
|
CE1
|
A:HIS127
|
4.8
|
18.0
|
1.0
|
OH
|
A:TYR118
|
4.9
|
20.1
|
1.0
|
CB
|
A:HIS193
|
5.0
|
11.9
|
1.0
|
C4
|
A:IMD302
|
5.0
|
20.0
|
1.0
|
|
Fluorine binding site 2 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 2 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F303
b:37.9
occ:1.00
|
F2
|
A:TFA303
|
0.0
|
37.9
|
1.0
|
C2
|
A:TFA303
|
1.4
|
25.2
|
1.0
|
F1
|
A:TFA303
|
2.2
|
32.4
|
1.0
|
F3
|
A:TFA303
|
2.2
|
26.9
|
1.0
|
C1
|
A:TFA303
|
2.4
|
20.4
|
1.0
|
O
|
A:TFA303
|
2.7
|
22.0
|
1.0
|
OH
|
A:TYR118
|
3.1
|
20.1
|
1.0
|
N
|
A:GLY195
|
3.5
|
16.7
|
1.0
|
OXT
|
A:TFA303
|
3.5
|
16.9
|
1.0
|
CB
|
A:TYR124
|
3.6
|
25.7
|
1.0
|
CD2
|
A:TYR124
|
3.6
|
26.2
|
1.0
|
CG
|
A:TYR124
|
3.8
|
19.9
|
1.0
|
C4
|
A:IMD302
|
3.8
|
20.0
|
1.0
|
CA
|
A:GLY195
|
3.8
|
16.1
|
1.0
|
C
|
A:GLY194
|
3.9
|
22.7
|
1.0
|
C5
|
A:IMD302
|
4.0
|
18.7
|
1.0
|
CE1
|
A:HIS127
|
4.1
|
18.0
|
1.0
|
N3
|
A:IMD302
|
4.3
|
16.2
|
1.0
|
CZ
|
A:TYR118
|
4.4
|
20.9
|
1.0
|
O
|
A:GLY194
|
4.4
|
14.9
|
1.0
|
CA
|
A:GLY194
|
4.5
|
18.0
|
1.0
|
CE2
|
A:TYR124
|
4.6
|
23.4
|
1.0
|
N1
|
A:IMD302
|
4.6
|
12.6
|
1.0
|
C2
|
A:IMD302
|
4.7
|
18.9
|
1.0
|
NE2
|
A:HIS127
|
4.7
|
16.1
|
1.0
|
CD1
|
A:ILE205
|
4.7
|
11.3
|
1.0
|
CD2
|
A:HIS193
|
4.8
|
15.9
|
1.0
|
CO
|
A:CO301
|
4.8
|
15.0
|
1.0
|
CD1
|
A:TYR124
|
4.9
|
25.0
|
1.0
|
O
|
A:TYR124
|
5.0
|
19.8
|
1.0
|
CA
|
A:TYR124
|
5.0
|
23.5
|
1.0
|
|
Fluorine binding site 3 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 3 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F303
b:26.9
occ:1.00
|
F3
|
A:TFA303
|
0.0
|
26.9
|
1.0
|
C2
|
A:TFA303
|
1.4
|
25.2
|
1.0
|
F2
|
A:TFA303
|
2.2
|
37.9
|
1.0
|
F1
|
A:TFA303
|
2.2
|
32.4
|
1.0
|
C1
|
A:TFA303
|
2.3
|
20.4
|
1.0
|
O
|
A:TFA303
|
3.0
|
22.0
|
1.0
|
OXT
|
A:TFA303
|
3.1
|
16.9
|
1.0
|
C2
|
A:IMD302
|
3.3
|
18.9
|
1.0
|
N1
|
A:IMD302
|
3.3
|
12.6
|
1.0
|
N3
|
A:IMD302
|
3.5
|
16.2
|
1.0
|
C5
|
A:IMD302
|
3.5
|
18.7
|
1.0
|
C4
|
A:IMD302
|
3.6
|
20.0
|
1.0
|
CG2
|
A:VAL147
|
3.7
|
11.8
|
1.0
|
CD1
|
A:ILE205
|
3.9
|
11.3
|
1.0
|
CG1
|
A:VAL147
|
4.3
|
8.5
|
1.0
|
OH
|
A:TYR118
|
4.4
|
20.1
|
1.0
|
CD2
|
A:HIS193
|
4.5
|
15.9
|
1.0
|
CO
|
A:CO301
|
4.5
|
15.0
|
1.0
|
CB
|
A:VAL147
|
4.6
|
9.4
|
1.0
|
CG2
|
A:THR159
|
4.6
|
12.2
|
1.0
|
OG1
|
A:THR159
|
4.8
|
10.9
|
1.0
|
NE2
|
A:HIS193
|
4.8
|
14.5
|
1.0
|
|
Fluorine binding site 4 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 4 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F305
b:22.3
occ:0.69
|
F1
|
D:TFA305
|
0.0
|
22.3
|
0.7
|
C2
|
D:TFA305
|
1.3
|
19.3
|
0.7
|
F2
|
D:TFA305
|
2.1
|
24.8
|
0.7
|
F3
|
D:TFA305
|
2.1
|
26.2
|
0.7
|
C1
|
D:TFA305
|
2.3
|
11.7
|
0.7
|
O
|
D:TFA305
|
2.9
|
10.7
|
0.7
|
OXT
|
D:TFA305
|
3.1
|
14.3
|
0.7
|
C5
|
D:IMD302
|
3.3
|
23.4
|
1.0
|
C4
|
D:IMD302
|
3.3
|
17.3
|
1.0
|
N1
|
D:IMD302
|
3.4
|
17.8
|
1.0
|
N3
|
D:IMD302
|
3.5
|
12.6
|
1.0
|
C2
|
D:IMD302
|
3.5
|
12.8
|
1.0
|
CG2
|
D:VAL147
|
3.8
|
11.0
|
1.0
|
CD1
|
D:ILE205
|
4.1
|
12.7
|
1.0
|
CG1
|
D:VAL147
|
4.4
|
11.7
|
1.0
|
CD2
|
D:HIS193
|
4.4
|
10.8
|
1.0
|
CO
|
D:CO301
|
4.6
|
12.1
|
1.0
|
OG1
|
D:THR159
|
4.6
|
15.3
|
1.0
|
OH
|
D:TYR118
|
4.6
|
17.4
|
1.0
|
CB
|
D:VAL147
|
4.7
|
11.9
|
1.0
|
CG2
|
D:THR159
|
4.7
|
9.1
|
1.0
|
NE2
|
D:HIS193
|
4.9
|
13.6
|
1.0
|
|
Fluorine binding site 5 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 5 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F305
b:24.8
occ:0.69
|
F2
|
D:TFA305
|
0.0
|
24.8
|
0.7
|
C2
|
D:TFA305
|
1.3
|
19.3
|
0.7
|
F3
|
D:TFA305
|
2.1
|
26.2
|
0.7
|
F1
|
D:TFA305
|
2.1
|
22.3
|
0.7
|
C1
|
D:TFA305
|
2.3
|
11.7
|
0.7
|
O
|
D:TFA305
|
2.7
|
10.7
|
0.7
|
O
|
D:GLY194
|
3.0
|
13.6
|
1.0
|
C
|
D:GLY194
|
3.1
|
17.2
|
1.0
|
N
|
D:GLY195
|
3.3
|
16.5
|
1.0
|
OXT
|
D:TFA305
|
3.4
|
14.3
|
0.7
|
CA
|
D:GLY195
|
3.7
|
17.0
|
1.0
|
CG2
|
D:THR159
|
3.8
|
9.1
|
1.0
|
CD2
|
D:HIS193
|
3.8
|
10.8
|
1.0
|
CA
|
D:GLY194
|
3.8
|
16.6
|
1.0
|
N
|
D:GLY194
|
4.2
|
16.1
|
1.0
|
OG1
|
D:THR159
|
4.2
|
15.3
|
1.0
|
CB
|
D:THR159
|
4.4
|
14.0
|
1.0
|
CA
|
D:THR159
|
4.4
|
13.2
|
1.0
|
C5
|
D:IMD302
|
4.5
|
23.4
|
1.0
|
N1
|
D:IMD302
|
4.6
|
17.8
|
1.0
|
CG
|
D:HIS193
|
4.7
|
12.0
|
1.0
|
C
|
D:HIS193
|
4.7
|
16.1
|
1.0
|
CE1
|
D:HIS127
|
4.8
|
13.8
|
1.0
|
NE2
|
D:HIS193
|
4.8
|
13.6
|
1.0
|
CB
|
D:HIS193
|
4.9
|
12.3
|
1.0
|
|
Fluorine binding site 6 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 6 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:F305
b:26.2
occ:0.69
|
F3
|
D:TFA305
|
0.0
|
26.2
|
0.7
|
C2
|
D:TFA305
|
1.3
|
19.3
|
0.7
|
F2
|
D:TFA305
|
2.1
|
24.8
|
0.7
|
F1
|
D:TFA305
|
2.1
|
22.3
|
0.7
|
C1
|
D:TFA305
|
2.3
|
11.7
|
0.7
|
OXT
|
D:TFA305
|
2.7
|
14.3
|
0.7
|
C5
|
D:IMD302
|
3.2
|
23.4
|
1.0
|
OH
|
D:TYR118
|
3.3
|
17.4
|
1.0
|
O
|
D:TFA305
|
3.5
|
10.7
|
0.7
|
N
|
D:GLY195
|
3.6
|
16.5
|
1.0
|
C4
|
D:IMD302
|
3.6
|
17.3
|
1.0
|
CB
|
D:TYR124
|
3.6
|
20.4
|
1.0
|
CD2
|
D:TYR124
|
3.7
|
25.7
|
1.0
|
CG
|
D:TYR124
|
3.8
|
16.5
|
1.0
|
N1
|
D:IMD302
|
3.9
|
17.8
|
1.0
|
CA
|
D:GLY195
|
4.0
|
17.0
|
1.0
|
C
|
D:GLY194
|
4.0
|
17.2
|
1.0
|
CE1
|
D:HIS127
|
4.1
|
13.8
|
1.0
|
N3
|
D:IMD302
|
4.5
|
12.6
|
1.0
|
O
|
D:GLY194
|
4.5
|
13.6
|
1.0
|
CE2
|
D:TYR124
|
4.5
|
24.9
|
1.0
|
CA
|
D:GLY194
|
4.5
|
16.6
|
1.0
|
CZ
|
D:TYR118
|
4.6
|
17.4
|
1.0
|
C2
|
D:IMD302
|
4.6
|
12.8
|
1.0
|
CD1
|
D:TYR124
|
4.6
|
16.4
|
1.0
|
CD2
|
D:HIS193
|
4.7
|
10.8
|
1.0
|
CO
|
D:CO301
|
4.8
|
12.1
|
1.0
|
NE2
|
D:HIS127
|
4.8
|
13.3
|
1.0
|
CD1
|
D:ILE205
|
5.0
|
12.7
|
1.0
|
|
Fluorine binding site 7 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 7 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:F303
b:28.6
occ:1.00
|
F1
|
C:TFA303
|
0.0
|
28.6
|
1.0
|
C2
|
C:TFA303
|
1.4
|
23.9
|
1.0
|
F2
|
C:TFA303
|
2.2
|
32.2
|
1.0
|
F3
|
C:TFA303
|
2.2
|
29.4
|
1.0
|
C1
|
C:TFA303
|
2.4
|
23.1
|
1.0
|
OXT
|
C:TFA303
|
2.8
|
18.8
|
1.0
|
O
|
C:GLY194
|
3.1
|
16.2
|
1.0
|
C
|
C:GLY194
|
3.2
|
20.3
|
1.0
|
N
|
C:GLY195
|
3.5
|
16.6
|
1.0
|
O
|
C:TFA303
|
3.5
|
24.3
|
1.0
|
CD2
|
C:HIS193
|
3.7
|
15.1
|
1.0
|
CA
|
C:GLY195
|
3.8
|
19.8
|
1.0
|
CA
|
C:GLY194
|
3.8
|
20.6
|
1.0
|
CG2
|
C:THR159
|
3.9
|
11.9
|
1.0
|
N
|
C:GLY194
|
4.2
|
22.8
|
1.0
|
OG1
|
C:THR159
|
4.3
|
15.8
|
1.0
|
CB
|
C:THR159
|
4.5
|
14.9
|
1.0
|
C5
|
C:IMD302
|
4.5
|
21.0
|
1.0
|
NE2
|
C:HIS193
|
4.6
|
19.0
|
1.0
|
CE1
|
C:HIS127
|
4.6
|
18.2
|
1.0
|
CG
|
C:HIS193
|
4.6
|
20.1
|
1.0
|
CA
|
C:THR159
|
4.7
|
12.9
|
1.0
|
N1
|
C:IMD302
|
4.7
|
10.7
|
1.0
|
C
|
C:HIS193
|
4.7
|
22.4
|
1.0
|
OH
|
C:TYR118
|
4.9
|
22.4
|
1.0
|
C4
|
C:IMD302
|
4.9
|
18.2
|
1.0
|
CO
|
C:CO301
|
4.9
|
16.2
|
1.0
|
CB
|
C:HIS193
|
5.0
|
16.0
|
1.0
|
CB
|
C:TYR124
|
5.0
|
25.8
|
1.0
|
|
Fluorine binding site 8 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 8 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:F303
b:32.2
occ:1.00
|
F2
|
C:TFA303
|
0.0
|
32.2
|
1.0
|
C2
|
C:TFA303
|
1.4
|
23.9
|
1.0
|
F1
|
C:TFA303
|
2.2
|
28.6
|
1.0
|
F3
|
C:TFA303
|
2.2
|
29.4
|
1.0
|
C1
|
C:TFA303
|
2.4
|
23.1
|
1.0
|
O
|
C:TFA303
|
2.7
|
24.3
|
1.0
|
C5
|
C:IMD302
|
3.2
|
21.0
|
1.0
|
OH
|
C:TYR118
|
3.2
|
22.4
|
1.0
|
C4
|
C:IMD302
|
3.2
|
18.2
|
1.0
|
OXT
|
C:TFA303
|
3.5
|
18.8
|
1.0
|
CD2
|
C:TYR124
|
3.6
|
25.6
|
1.0
|
CB
|
C:TYR124
|
3.8
|
25.8
|
1.0
|
N1
|
C:IMD302
|
3.9
|
10.7
|
1.0
|
CG
|
C:TYR124
|
3.9
|
22.8
|
1.0
|
N3
|
C:IMD302
|
4.0
|
14.1
|
1.0
|
CE1
|
C:HIS127
|
4.1
|
18.2
|
1.0
|
N
|
C:GLY195
|
4.2
|
16.6
|
1.0
|
C2
|
C:IMD302
|
4.3
|
19.7
|
1.0
|
CE2
|
C:TYR124
|
4.4
|
30.0
|
1.0
|
CA
|
C:GLY195
|
4.5
|
19.8
|
1.0
|
C
|
C:GLY194
|
4.5
|
20.3
|
1.0
|
CZ
|
C:TYR118
|
4.5
|
24.4
|
1.0
|
CD1
|
C:ILE205
|
4.5
|
14.2
|
1.0
|
CO
|
C:CO301
|
4.6
|
16.2
|
1.0
|
NE2
|
C:HIS127
|
4.8
|
20.1
|
1.0
|
CD2
|
C:HIS193
|
4.8
|
15.1
|
1.0
|
O
|
C:GLY194
|
4.8
|
16.2
|
1.0
|
CD1
|
C:TYR124
|
4.9
|
22.4
|
1.0
|
|
Fluorine binding site 9 out
of 9 in 5v7y
Go back to
Fluorine Binding Sites List in 5v7y
Fluorine binding site 9 out
of 9 in the Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 9 of Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:F303
b:29.4
occ:1.00
|
F3
|
C:TFA303
|
0.0
|
29.4
|
1.0
|
C2
|
C:TFA303
|
1.4
|
23.9
|
1.0
|
F1
|
C:TFA303
|
2.2
|
28.6
|
1.0
|
F2
|
C:TFA303
|
2.2
|
32.2
|
1.0
|
C1
|
C:TFA303
|
2.3
|
23.1
|
1.0
|
OXT
|
C:TFA303
|
3.0
|
18.8
|
1.0
|
O
|
C:TFA303
|
3.2
|
24.3
|
1.0
|
N3
|
C:IMD302
|
3.5
|
14.1
|
1.0
|
C2
|
C:IMD302
|
3.5
|
19.7
|
1.0
|
C4
|
C:IMD302
|
3.5
|
18.2
|
1.0
|
CG2
|
C:VAL147
|
3.6
|
14.8
|
1.0
|
C5
|
C:IMD302
|
3.6
|
21.0
|
1.0
|
N1
|
C:IMD302
|
3.6
|
10.7
|
1.0
|
CG1
|
C:VAL147
|
4.0
|
16.0
|
1.0
|
CD1
|
C:ILE205
|
4.2
|
14.2
|
1.0
|
CB
|
C:VAL147
|
4.3
|
12.6
|
1.0
|
CD2
|
C:HIS193
|
4.4
|
15.1
|
1.0
|
OG1
|
C:THR159
|
4.5
|
15.8
|
1.0
|
CG2
|
C:THR159
|
4.5
|
11.9
|
1.0
|
CO
|
C:CO301
|
4.6
|
16.2
|
1.0
|
NE2
|
C:HIS193
|
4.8
|
19.0
|
1.0
|
OH
|
C:TYR118
|
4.9
|
22.4
|
1.0
|
|
Reference:
N.J.Schnicker,
M.Razzaghi,
S.Guha Thakurta,
S.Chakravarthy,
M.Dey.
Bacillus Anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu. Biochemistry V. 56 5771 2017.
ISSN: ISSN 1520-4995
PubMed: 28981257
DOI: 10.1021/ACS.BIOCHEM.7B00601
Page generated: Thu Aug 1 15:58:17 2024
|